The two distinctive metal ion binding domains of the wheat metallothionein Ec-1

NMR Spectroscopy in Bioinorganic Chemistry

“…[42,43] Common replacing the N3H protons of the thymine nucleobases. [44] Not until 40 years later, Tanaka et al could finally prove this assumption using 15 N NMR spectroscopy. [45] Upon addition of Hg Our recent studies showed that also RNA sequences comprising 2, 3, 6, 10, and up to 20 consecutive uridine residues can incorporate Hg 2+ ions into the helix forming U-Hg 2+ -U base pairs without disturbing the A-helical structure.…”

“…[49] NMR spectroscopy has been extensively used over the past years to evaluate the binding mode of metal complexes to nucleic acids. For example, [ 1 H, 15 N]-HSQC experiments were used to obtain insights into the mechanism of action of platinum drugs, including kinetics and selectivity of DNA platination reactions. [50] Also [ Pt chemical shift range spans thousands of ppm and is particularly sensitive to changes in the coordination sphere.…”

“…6A). [15] Cd]-COSY experiments direct coupling of metal ions can be observed and hence allows the identification of metal ions that belong to the same cluster. [55] In Cys 6 cluster (C) that was recently discovered in the γ-domain of the plant MT E c -1.…”

“…Nuclear magnetic resonance (NMR) spectroscopy is a crucial technique that we use not only to obtain structural information on our molecules at an atomic level [6][7][8][9][10][11] but, even more important, to elucidate in detail their metal ion binding. [2,9,10,[12][13][14][15][16][17][18] Fig. 1 shows three examples of recently solved structures, belonging to the three families of biomolecules we are working with: the exon/intron binding site 1 (EBS1/IBS1; PDB ID 2K65) [19] of the yeast mitochondrial group II intron Sc.ai5γ, a silver modified duplex DNA (PDB ID 2KE8), [8] and the C-terminal domain of the seed-specific wheat MT Zn 6 E c -1, denoted as Zn 4 β E -E c -1 (PDB ID 2KAK).…”

“…[10] The chemical institutes at the University of Zurich run a central NMR facility currently equipped with one 700, one 600, three 500, two 400, and one 300 MHz spectrometer. Three of the high-field machines (500, 600, and 700 MHz) are equipped with z-axis pulsed field gradient Cryoprobes TM (Bruker), and are used for classical structural biology experiments (2D and 3D experiments on 1 H, 13 C, 15 N nuclei, as well as 31 P). One 500 MHz spectrometer is dedicated to variable-temperature and multinuclear NMR studies.…”